|
In biochemistry, receptor–ligand kinetics is a branch of chemical kinetics in which the kinetic species are defined by different non-covalent bindings and/or conformations of the molecules involved, which are denoted as ''receptor(s)'' and ''ligand(s)''. Receptor–ligand binding kinetics also involves the on- and off-rates of binding. A main goal of receptor–ligand kinetics is to determine the concentrations of the various kinetic species (i.e., the states of the receptor and ligand) at all times, from a given set of initial concentrations and a given set of rate constants. In a few cases, an analytical solution of the rate equations may be determined, but this is relatively rare. However, most rate equations can be integrated numerically, or approximately, using the steady-state approximation. A less ambitious goal is to determine the final ''equilibrium'' concentrations of the kinetic species, which is adequate for the interpretation of equilibrium binding data. A converse goal of receptor–ligand kinetics is to estimate the rate constants and/or dissociation constants of the receptors and ligands from experimental kinetic or equilibrium data. The total concentrations of receptor and ligands are sometimes varied systematically to estimate these constants. == Binding kinetics == The binding constant is a special case of the equilibrium constant . It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: :. The reaction is characterized by the on-rate constant and the off-rate constant , which have units of 1/(concentration time) and 1/time, respectively. In equilibrium, the forward binding transition should be balanced by the backward unbinding transition . That is, :, 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Receptor–ligand kinetics」の詳細全文を読む スポンサード リンク
|